Journal
JOURNAL OF BIOMOLECULAR NMR
Volume 24, Issue 2, Pages 143-148Publisher
KLUWER ACADEMIC PUBL
DOI: 10.1023/A:1020948529076
Keywords
asymmetry; protein dimer; protein structure; pseudocontact shifts; residual dipolar coupling
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We demonstrate a novel methodology to disrupt the symmetry in the NMR spectra of homodimers. A paramagnetic probe is introduced sub-stoichiometrically to create an asymmetric system with the paramagnetic probe residing on only one monomer within the dimer. This creates sufficient magnetic anisotropy for resolution of symmetry-related overlapped resonances and, consequently, detection of pseudocontact shifts and residual dipolar couplings specific to each monomeric component. These pseudocontact shifts can be readily incorporated into existing structure refinement calculations and enable determination of monomer orientation within the dimeric protein. This methodology can be widely used for solution structure determination of symmetric dimers.
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